[Purification and some properties of 1,3-1,4-beta-glucanase from Bacillus subtilis].
Using chromatography on cellulose, SE-Sephadex G-50 and gel filtration on acrylex P-60, 1.3 -- 1.4-beta-glucanase from Bac. subtilis, strain 103 was obtained and purified 142-fold. The specific activity of the purified enzyme was 18.5 units per mg of protein. The homogeneity of 1.3 -- 1.4-beta-glucanase was determined by gel filtration on acrylex P-60, polyacrylamide gel electrophoresis, isoelectrofocusing and ultracentrifugation. Using electrophoresis in Na-SDS and gel filtration on acrylex P-60, the molecular weight of the enzyme was found to be equal to 30 000 and 33 000, respectively. The isoelectric point for the enzyme lies at pH 5.4. The enzyme does not contain tryptophane, free SH-groups or carbohydrates.
D001412:Bacillus subtilis / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D014364:Tryptophan / Q000032:analysis
D014364:Tryptophan; D006026:Glycoside Hydrolases; C028020:licheninase
Ochistka i nekotorye svoĩstva 1,3-1,4-beta-gliukanazy iz Bacillus subtilis.